Q81LV1 (END4_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable endonuclease 4
EC=3.1.21.2

Alternative name(s):
Endodeoxyribonuclease IV
Endonuclease IV

Gene names

Name:	nfo
Ordered Locus Names:	BA_4508, GBAA_4508, BAS4186

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin By similarity. HAMAP MF_00152
Catalytic activity	Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. HAMAP MF_00152
Cofactor	Binds 3 zinc ions By similarity. HAMAP MF_00152
Sequence similarities	Belongs to the AP endonuclease 2 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro deoxyribonuclease IV (phage-T4-induced) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 298

298

Probable endonuclease 4 HAMAP MF_00152

PRO_0000190819

Sites

Metal binding

69

1

Zinc 1 By similarity

Metal binding

111

1

Zinc 1 By similarity

Metal binding

146

1

Zinc 1 By similarity

Metal binding

146

1

Zinc 2 By similarity

Metal binding

180

1

Zinc 2 By similarity

Metal binding

183

1

Zinc 3 By similarity

Metal binding

215

1

Zinc 2 By similarity

Metal binding

228

1

Zinc 3 By similarity

Metal binding

230

1

Zinc 3 By similarity

Metal binding

260

1

Zinc 2 By similarity

Secondary structure

1

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298

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Beta strand

12 – 14

3

Helix

16 – 24

9

Turn

25 – 27

3

Beta strand

29 – 33

5

Helix

46 – 49

4

Helix

51 – 60

10

Beta strand

66 – 69

4

Helix

82 – 101

20

Beta strand

102 – 104

3

Beta strand

107 – 110

4

Helix

120 – 134

15

Beta strand

140 – 146

7

Helix

159 – 168

10

Helix

172 – 174

3

Beta strand

175 – 180

6

Helix

181 – 186

6

Helix

191 – 205

15

Helix

208 – 210

3

Beta strand

211 – 216

6

Beta strand

218 – 221

4

Beta strand

235 – 238

4

Helix

240 – 247

8

Helix

250 – 252

3

Beta strand

257 – 259

3

Beta strand

267 – 269

3

Helix

275 – 284

10

Helix

291 – 296

6

Sequences

	Sequence		Length	Mass (Da)
	Q81LV1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: C5178AB085784C8A	FASTA	298	32,909
	10 20 30 40 50 60 MLKIGSHVSM SGKKMLLAAS EEAVSYGATT FMIYTGAPQN TRRKPIEELN IEAGRKHMEQ 70 80 90 100 110 120 NGIEEIIVHA PYIINVGNTT KPETFQLGVD FLRMEIERTS ALGVAKQIVL HPGAHVGAGA 130 140 150 160 170 180 DAGIQQIIKG LNEVLTPDQT VNIALETMAG KGTECGRSFE EIAKIIDGVK YNEKLSVCFD 190 200 210 220 230 240 TCHTHDAGYD IVNNFDGVLN EFDKIVGIDR LQVLHINDSK NVRGAGKDRH ENIGFGHIGY 250 260 270 280 290 KALHHIVHHP QLTHVPKILE TPYVGEDKKD KKPPYKLEIE MLKNGTFDEG LLEKIKAQ

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP28219.1.
AE017334 Genomic DNA. Translation: AAT33627.1.
AE017225 Genomic DNA. Translation: AAT56486.1.

RefSeq

NP_846733.1. NC_003997.3.
YP_021152.1. NC_007530.2.
YP_030435.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XP3	X-ray	2.57	A	1-298	[»]

ProteinModelPortal

Q81LV1.

SMR

Q81LV1. Positions 2-298.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000012226; EBBACP00000011982; EBBACG00000012218.
EBBACT00000013675; EBBACP00000013296; EBBACG00000013667.
EBBACT00000019466; EBBACP00000018951; EBBACG00000019457.

GeneID

1088232.
2818504.
2852108.

GenomeReviews

Gene locus BA_4508 in contig AE016879_GR.
Gene locus BAS4186 in contig AE017225_GR.
Gene locus GBAA_4508 in contig AE017334_GR.

KEGG

ban:BA_4508.
bar:GBAA_4508.
bat:BAS4186.

TIGR

BA_4508.
GBAA_4508.

Phylogenomic databases

GeneTree

EBGT00050000001754.

HOGENOM

HBG565018.

OMA

QIALETM.

ProtClustDB

PRK01060.

Enzyme and pathway databases

BioCyc

BANT260799:BAS4186-MONOMER.
BANT261594:GBAA4508-MONOMER.

Family and domain databases

HAMAP

MF_00152. Nfo.
[Tree]

InterPro

IPR018246. AP_endonuc_F2_Zn_BS.
IPR001719. Endodeoxyribonuclease_IV.
IPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase_TIM-brl.
[Graphical view]

Gene3D

G3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit.

KO

K01151.

PANTHER

PTHR21445. AP_endnuclease2. 1 hit.

Pfam

PF01261. AP_endonuc_2. 1 hit.
[Graphical view]

SMART

SM00518. AP2Ec. 1 hit.
[Graphical view]

SUPFAM

SSF51658. Xyl_isomerase-like_TIM-brl. 1 hit.

TIGRFAMs

TIGR00587. Nfo. 1 hit.

PROSITE

PS00729. AP_NUCLEASE_F2_1. 1 hit.
PS00730. AP_NUCLEASE_F2_2. 1 hit.
PS00731. AP_NUCLEASE_F2_3. 1 hit.
PS51432. AP_NUCLEASE_F2_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

END4_BACAN

Accession

Primary (citable) accession number: Q81LV1
Secondary accession number(s): Q6HTA3, Q6KMJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program